Studies on Purification and Properties of Superoxide Dismutase from Geese Erythrocytes

Abstract

Abstract: Copperzinc superoxide dismutase (Cu,Zn-SOD) from geese erythrocytes has been purified by chloroform-ethanol fractionation, acetone precipitation and DE-32 chromatography. The results showed that the specific activity of the enzyme was 10656.14Umg, and its purification factor was 354.73. This enzyme had two identical subunits. The molecular weight was about 32000, and the identical subunit molecular weigh about 16000. And the ultraviolet absorption peak of the enzyme was found at 258nm .The enzyme was sensitive to KCN and H2O2, the enzyme optimum pH was from 6 to 9, stable below 60℃.

Key words: geese erythrocytes, Cu,Zn-SOD, purification, property

ZHANG Lan-Jie, XIN Guang, ZHANG Wei-Hua, YUAN Qin-Sheng. Studies on Purification and Properties of Superoxide Dismutase from Geese Erythrocytes[J]. FOOD SCIENCE, 2005, 26(12): 86-89.

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Studies on Purification and Properties of Superoxide Dismutase from Geese Erythrocytes

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